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GABAB receptor cell-surface export is controlled by an endoplasmic reticulum gatekeeper
Endoplasmic reticulum (ER) release and cell-surface export of many G protein-coupled receptors (GPCRs) are tightly regulated. For gamma-aminobutyric acid (GABA) B receptors of GABA, the major mammalian inhibitory neurotransmitter, the ligand-binding GB1 subunit is maintained in the ER by unknown mec...
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| Published in: | Molecular psychiatry 2016-04, Vol.21 (4), p.480-490 |
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| Main Authors: | , , , , , , , , , , , , , , , , |
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| container_title | Molecular psychiatry |
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| creator | Doly, S Shirvani, H Gäta, G Meye, F J Emerit, M-B Enslen, H Achour, L Pardo-Lopez, L Yang, S-K Armand, V Gardette, R Giros, B Gassmann, M Bettler, B Mameli, M Darmon, M Marullo, S |
| description | Endoplasmic reticulum (ER) release and cell-surface export of many G protein-coupled receptors (GPCRs) are tightly regulated. For gamma-aminobutyric acid (GABA)
B
receptors of GABA, the major mammalian inhibitory neurotransmitter, the ligand-binding GB1 subunit is maintained in the ER by unknown mechanisms in the absence of hetero-dimerization with the GB2 subunit. We report that GB1 retention is regulated by a specific gatekeeper, PRAF2. This ER resident transmembrane protein binds to GB1, preventing its progression in the biosynthetic pathway. GB1 release occurs upon competitive displacement from PRAF2 by GB2. PRAF2 concentration, relative to that of GB1 and GB2, tightly controls cell-surface receptor density and controls GABA
B
function in neurons. Experimental perturbation of PRAF2 levels
in vivo
caused marked hyperactivity disorders in mice. These data reveal an unanticipated major impact of specific ER gatekeepers on GPCR function and identify PRAF2 as a new molecular target with therapeutic potential for psychiatric and neurological diseases involving GABA
B
function. |
| doi_str_mv | 10.1038/mp.2015.72 |
| format | article |
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B
receptors of GABA, the major mammalian inhibitory neurotransmitter, the ligand-binding GB1 subunit is maintained in the ER by unknown mechanisms in the absence of hetero-dimerization with the GB2 subunit. We report that GB1 retention is regulated by a specific gatekeeper, PRAF2. This ER resident transmembrane protein binds to GB1, preventing its progression in the biosynthetic pathway. GB1 release occurs upon competitive displacement from PRAF2 by GB2. PRAF2 concentration, relative to that of GB1 and GB2, tightly controls cell-surface receptor density and controls GABA
B
function in neurons. Experimental perturbation of PRAF2 levels
in vivo
caused marked hyperactivity disorders in mice. These data reveal an unanticipated major impact of specific ER gatekeepers on GPCR function and identify PRAF2 as a new molecular target with therapeutic potential for psychiatric and neurological diseases involving GABA
B
function.</description><identifier>ISSN: 1359-4184</identifier><identifier>EISSN: 1476-5578</identifier><identifier>DOI: 10.1038/mp.2015.72</identifier><identifier>PMID: 26033241</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>13/109 ; 13/31 ; 13/51 ; 13/89 ; 13/95 ; 14/19 ; 38/35 ; 631/80 ; 64/60 ; 9/74 ; Amino Acid Sequence ; Animals ; Behavioral Sciences ; Biochemistry, Molecular Biology ; Biological Psychology ; Carrier Proteins - metabolism ; Cell Line ; Cell Membrane - metabolism ; Cell surface ; Dimerization ; Endoplasmic reticulum ; Endoplasmic Reticulum - metabolism ; G protein-coupled receptors ; gamma-Aminobutyric Acid - metabolism ; HEK293 Cells ; Humans ; Hyperactivity ; Life Sciences ; Medicine ; Medicine & Public Health ; Membrane Proteins - metabolism ; Mice ; Mice, Knockout ; Neurological diseases ; Neurosciences ; Neurotransmitters ; original-article ; Pharmacotherapy ; Protein Multimerization ; Protein Subunits ; Protein transport ; Proteins ; Psychiatry ; Receptor density ; Receptors, GABA-B - metabolism ; Retention ; γ-Aminobutyric acid ; γ-Aminobutyric acid B receptors</subject><ispartof>Molecular psychiatry, 2016-04, Vol.21 (4), p.480-490</ispartof><rights>Macmillan Publishers Limited 2016</rights><rights>Copyright Nature Publishing Group Apr 2016</rights><rights>Macmillan Publishers Limited 2016.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3522-ccaa574b185b10c4a0647af3af1cdd5e100e2ac8d78f8ff933d26d723d817623</citedby><cites>FETCH-LOGICAL-c3522-ccaa574b185b10c4a0647af3af1cdd5e100e2ac8d78f8ff933d26d723d817623</cites><orcidid>0000-0001-9741-5293 ; 0000-0002-3517-8605 ; 0000-0001-9604-9973 ; 0000-0001-5876-9822</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26033241$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://inserm.hal.science/inserm-01153352$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Doly, S</creatorcontrib><creatorcontrib>Shirvani, H</creatorcontrib><creatorcontrib>Gäta, G</creatorcontrib><creatorcontrib>Meye, F J</creatorcontrib><creatorcontrib>Emerit, M-B</creatorcontrib><creatorcontrib>Enslen, H</creatorcontrib><creatorcontrib>Achour, L</creatorcontrib><creatorcontrib>Pardo-Lopez, L</creatorcontrib><creatorcontrib>Yang, S-K</creatorcontrib><creatorcontrib>Armand, V</creatorcontrib><creatorcontrib>Gardette, R</creatorcontrib><creatorcontrib>Giros, B</creatorcontrib><creatorcontrib>Gassmann, M</creatorcontrib><creatorcontrib>Bettler, B</creatorcontrib><creatorcontrib>Mameli, M</creatorcontrib><creatorcontrib>Darmon, M</creatorcontrib><creatorcontrib>Marullo, S</creatorcontrib><title>GABAB receptor cell-surface export is controlled by an endoplasmic reticulum gatekeeper</title><title>Molecular psychiatry</title><addtitle>Mol Psychiatry</addtitle><addtitle>Mol Psychiatry</addtitle><description>Endoplasmic reticulum (ER) release and cell-surface export of many G protein-coupled receptors (GPCRs) are tightly regulated. For gamma-aminobutyric acid (GABA)
B
receptors of GABA, the major mammalian inhibitory neurotransmitter, the ligand-binding GB1 subunit is maintained in the ER by unknown mechanisms in the absence of hetero-dimerization with the GB2 subunit. We report that GB1 retention is regulated by a specific gatekeeper, PRAF2. This ER resident transmembrane protein binds to GB1, preventing its progression in the biosynthetic pathway. GB1 release occurs upon competitive displacement from PRAF2 by GB2. PRAF2 concentration, relative to that of GB1 and GB2, tightly controls cell-surface receptor density and controls GABA
B
function in neurons. Experimental perturbation of PRAF2 levels
in vivo
caused marked hyperactivity disorders in mice. These data reveal an unanticipated major impact of specific ER gatekeepers on GPCR function and identify PRAF2 as a new molecular target with therapeutic potential for psychiatric and neurological diseases involving GABA
B
function.</description><subject>13/109</subject><subject>13/31</subject><subject>13/51</subject><subject>13/89</subject><subject>13/95</subject><subject>14/19</subject><subject>38/35</subject><subject>631/80</subject><subject>64/60</subject><subject>9/74</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Behavioral Sciences</subject><subject>Biochemistry, Molecular Biology</subject><subject>Biological Psychology</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Line</subject><subject>Cell Membrane - metabolism</subject><subject>Cell surface</subject><subject>Dimerization</subject><subject>Endoplasmic reticulum</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>G protein-coupled receptors</subject><subject>gamma-Aminobutyric Acid - metabolism</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Hyperactivity</subject><subject>Life Sciences</subject><subject>Medicine</subject><subject>Medicine & Public Health</subject><subject>Membrane Proteins - 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Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Molecular psychiatry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Doly, S</au><au>Shirvani, H</au><au>Gäta, G</au><au>Meye, F J</au><au>Emerit, M-B</au><au>Enslen, H</au><au>Achour, L</au><au>Pardo-Lopez, L</au><au>Yang, S-K</au><au>Armand, V</au><au>Gardette, R</au><au>Giros, B</au><au>Gassmann, M</au><au>Bettler, B</au><au>Mameli, M</au><au>Darmon, M</au><au>Marullo, S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>GABAB receptor cell-surface export is controlled by an endoplasmic reticulum gatekeeper</atitle><jtitle>Molecular psychiatry</jtitle><stitle>Mol Psychiatry</stitle><addtitle>Mol Psychiatry</addtitle><date>2016-04</date><risdate>2016</risdate><volume>21</volume><issue>4</issue><spage>480</spage><epage>490</epage><pages>480-490</pages><issn>1359-4184</issn><eissn>1476-5578</eissn><abstract>Endoplasmic reticulum (ER) release and cell-surface export of many G protein-coupled receptors (GPCRs) are tightly regulated. For gamma-aminobutyric acid (GABA)
B
receptors of GABA, the major mammalian inhibitory neurotransmitter, the ligand-binding GB1 subunit is maintained in the ER by unknown mechanisms in the absence of hetero-dimerization with the GB2 subunit. We report that GB1 retention is regulated by a specific gatekeeper, PRAF2. This ER resident transmembrane protein binds to GB1, preventing its progression in the biosynthetic pathway. GB1 release occurs upon competitive displacement from PRAF2 by GB2. PRAF2 concentration, relative to that of GB1 and GB2, tightly controls cell-surface receptor density and controls GABA
B
function in neurons. Experimental perturbation of PRAF2 levels
in vivo
caused marked hyperactivity disorders in mice. These data reveal an unanticipated major impact of specific ER gatekeepers on GPCR function and identify PRAF2 as a new molecular target with therapeutic potential for psychiatric and neurological diseases involving GABA
B
function.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>26033241</pmid><doi>10.1038/mp.2015.72</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0001-9741-5293</orcidid><orcidid>https://orcid.org/0000-0002-3517-8605</orcidid><orcidid>https://orcid.org/0000-0001-9604-9973</orcidid><orcidid>https://orcid.org/0000-0001-5876-9822</orcidid><oa>free_for_read</oa></addata></record> |
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| language | eng |
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| source | Springer Nature |
| subjects | 13/109 13/31 13/51 13/89 13/95 14/19 38/35 631/80 64/60 9/74 Amino Acid Sequence Animals Behavioral Sciences Biochemistry, Molecular Biology Biological Psychology Carrier Proteins - metabolism Cell Line Cell Membrane - metabolism Cell surface Dimerization Endoplasmic reticulum Endoplasmic Reticulum - metabolism G protein-coupled receptors gamma-Aminobutyric Acid - metabolism HEK293 Cells Humans Hyperactivity Life Sciences Medicine Medicine & Public Health Membrane Proteins - metabolism Mice Mice, Knockout Neurological diseases Neurosciences Neurotransmitters original-article Pharmacotherapy Protein Multimerization Protein Subunits Protein transport Proteins Psychiatry Receptor density Receptors, GABA-B - metabolism Retention γ-Aminobutyric acid γ-Aminobutyric acid B receptors |
| title | GABAB receptor cell-surface export is controlled by an endoplasmic reticulum gatekeeper |
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